Imperial College London
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ProfessorThomasMeier

Faculty of Natural Sciences, Department of Life Sciences

Visiting Professor
 
 
 
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Contact

 

t.meier Website

 
 
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Location

 

501Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Schulz:2017:10.15252/embr.201643374,
author = {Schulz, S and Wilkes, M and Mills, DJ and Kühlbrandt, W and Meier, TK},
doi = {10.15252/embr.201643374},
journal = {Embo Reports},
pages = {526--535},
title = {Molecular architecture of the N type ATPase rotor ring from Burkholderia pseudomallei},
url = {http://dx.doi.org/10.15252/embr.201643374},
volume = {18},
year = {2017}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - The genome of the highly infectious bacterium Burkholderia pseudomallei harbours an atp-operon that encodes an N-type rotary ATPase, in addition to an operon for a regular F-type rotary ATPase. The molecular architecture of N-type ATPases is unknown and their biochemical properties and cellular functions are largely unexplored. We studied the B. pseudomallei N1No-type ATPase and investigated the structure and ion specificity of its membrane-embedded c-ring rotor by single-particle electron cryo-microscopy. Of several amphiphilic compounds tested for solubilizing the complex, the choice of the low-density, low-CMC detergent LDAO was optimal in terms of map quality and resolution. The cryoEM map of the c-ring at 6.1 Å resolution reveals a heptadecameric oligomer with a molecular mass of ~141 kDa. Biochemical measurements indicate that the c17 ring is H+ specific, demonstrating that the ATPase is proton-coupled. The c17 ring stoichiometry results in a very high ion-to-ATP ratio of 5.7. We propose that this N-ATPase is a highly efficient proton pump that helps these melioidosis-causing bacteria to survive in the hostile, acidic environment of phagosomes.
AU  - Schulz,S
AU  - Wilkes,M
AU  - Mills,DJ
AU  - Kühlbrandt,W
AU  - Meier,TK
DO  - 10.15252/embr.201643374
EP  - 535
PY  - 2017///
SN  - 1469-3178
SP  - 526
TI  - Molecular architecture of the N type ATPase rotor ring from Burkholderia pseudomallei
T2  - Embo Reports
UR  - http://dx.doi.org/10.15252/embr.201643374
UR  - http://hdl.handle.net/10044/1/44452
VL  - 18
ER  -
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